Dual-topology insertion of a dual-topology membrane protein

Nicholas B. Woodall, Ying Yin and James U. Bowie ()
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Nicholas B. Woodall: UCLA-DOE Institute, Molecular Biology Institute, University of California, Los Angeles
Ying Yin: UCLA-DOE Institute, Molecular Biology Institute, University of California, Los Angeles
James U. Bowie: UCLA-DOE Institute, Molecular Biology Institute, University of California, Los Angeles

Nature Communications, 2015, vol. 6, issue 1, 1-8

Abstract: Abstract Some membrane transporters are dual-topology dimers in which the subunits have inverted transmembrane topology. How a cell manages to generate equal populations of two opposite topologies from the same polypeptide chain remains unclear. For the dual-topology transporter EmrE, the evidence to date remains consistent with two extreme models. A post-translational model posits that topology remains malleable after synthesis and becomes fixed once the dimer forms. A second, co-translational model, posits that the protein inserts in both topologies in equal proportions. Here we show that while there is at least some limited topological malleability, the co-translational model likely dominates under normal circumstances.

Date: 2015
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DOI: 10.1038/ncomms9099

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